Kiril Mishev, Qing Lu, Bram Denoo, François Peurois, Wim Dejonghe, Jan Hullaert, Riet De Rycke, Sjef Boeren, Marine Bretou, Steven De Munck, Isha Sharma, Kaija Goodman, Kamila Kalinowska, Veronique Storme, Le Son Long Nguyen, Andrzej Drozdzecki, Sara Martins, Wim Nerinckx, Dominique Audenaert, Grégory Vert, Annemieke Madder, Marisa S Otegui, Erika Isono, Savvas N Savvides, Wim Annaert, Sacco De Vries, Jacqueline Cherfils, Johan Winne, Eugenia Russinova
Small GTP-binding proteins from the ADP-ribosylation factor (ARF) family are important regulators of vesicle formation and cellular trafficking in all eukaryotes. ARF activation is accomplished by a protein family of guanine nucleotide exchange factors (GEFs) that contain a conserved catalytic Sec7 domain. Here, we identified and characterized Secdin, a small-molecule inhibitor of Arabidopsis thaliana ARF-GEFs. Secdin application caused aberrant retention of plasma membrane (PM) proteins in late endosomal compartments, enhanced vacuolar degradation, impaired protein recycling, and delayed secretion and endocytosis...
October 2018: Plant Cell